MSHA_PAEAT
ID MSHA_PAEAT Reviewed; 408 AA.
AC A1R8N8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=D-inositol 3-phosphate glycosyltransferase;
DE EC=2.4.1.250 {ECO:0000255|HAMAP-Rule:MF_01695};
DE AltName: Full=N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_01695};
DE Short=GlcNAc-Ins-P N-acetylglucosaminyltransferase {ECO:0000255|HAMAP-Rule:MF_01695};
GN Name=mshA {ECO:0000255|HAMAP-Rule:MF_01695}; OrderedLocusNames=AAur_2891;
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=290340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1;
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
CC -!- FUNCTION: Catalyzes the transfer of a N-acetyl-glucosamine moiety to
CC 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-
CC deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis
CC pathway. {ECO:0000255|HAMAP-Rule:MF_01695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-glucosamine
CC = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-
CC phosphate + H(+) + UDP; Xref=Rhea:RHEA:26188, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58401,
CC ChEBI:CHEBI:58892; EC=2.4.1.250; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01695};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01695}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01695}.
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DR EMBL; CP000474; ABM08761.1; -; Genomic_DNA.
DR AlphaFoldDB; A1R8N8; -.
DR SMR; A1R8N8; -.
DR STRING; 290340.AAur_2891; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; ABM08761; ABM08761; AAur_2891.
DR KEGG; aau:AAur_2891; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_2_3_11; -.
DR OMA; HTMAKVK; -.
DR Proteomes; UP000000637; Chromosome.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102710; F:D-inositol-3-phosphate glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010125; P:mycothiol biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01695; MshA; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR InterPro; IPR017814; Mycothiol_biosynthesis_MshA.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR03449; mycothiol_MshA; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..408
FT /note="D-inositol 3-phosphate glycosyltransferase"
FT /id="PRO_0000400109"
FT BINDING 7
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 13..14
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 18..23
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 21
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 76
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 109
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 133
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 153
FT /ligand="1D-myo-inositol 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58401"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 227
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 232
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 288
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 310
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 318
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01695"
SQ SEQUENCE 408 AA; 44654 MW; 6677D1728B4A3008 CRC64;
MAFLSLHTSP MEQPGAGDAG GMNVYVRALA MALAESGVEV EIFTRSTKAG QPAVEHPGPG
VCVHNVMAGP RRKLPKEELP ELLHHMVEEI DRIRLQQLHG RYDAIHSHYW VSGVAGLELS
ELWGVPLVHT MHTMAKVKNL VLESGERPEP RRREEGEQRI VDGAARLVAN TPAEADELVS
HYGADLDRID VAPPGVDLKV FTPSFRRKSR SLRGVRPDSF HILFAGRIQR LKGPQVFVKA
AGILRKRRPD IDLEMTILGS LSGAKDFNLQ HFIEDAGLAD VVTHRPPVVA PELASWFRSA
DVVVMPSFSE SFGLVALEAQ ACGTPVVATN VGGLSRAISD GRTGILVDGH HPSDWADALE
DLYDDVQTRE DMGRLAATHA ESFGWQRTAA ITLESYREAV SGLLVPRR
